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Productin of functional galacto-oligosccharides using transfer action of -galactosidase

Research Project

Project/Area Number 62560126
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field 製造化学・食品
Research InstitutionKyoto University

Principal Investigator

MATSUNO Ryuichi  Faculty of Agriculture, Kyoto University, 農学部, 教授 (30032931)

Co-Investigator(Kenkyū-buntansha) NAKANISHI Kazuhiro  Faculty of Engineering, Okayama University, 工学部, 教授 (90026584)
Project Period (FY) 1987 – 1988
Project Status Completed (Fiscal Year 1988)
Budget Amount *help
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1988: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1987: ¥1,600,000 (Direct Cost: ¥1,600,000)
Keywords-galactosidase / Galacto-oligosaccharides / Transfer action / Enzyme modification / Immobilized enzyme / Bacillus circulans / バイオリアクター / β-ガラクトシダーゼ
Research Abstract

Lactose is less soluble compared with other saccharides and tras calcium ion. These properties are the demerit in the food manufacturing and the food additive production using milk and chese whey. To add a function as bifidus factor as well as to diminish the above demerit, the preseht study aimed at the effective production of galacto-oligosaccharides using -galactosidase 1( -gal 1) and -galactosidase 2 ( -Gal 2) from Bacillus circulans which have high activity for hydrolysis of lactose and for hydrolysis of lactose and for synthesis of galactooligosaccharide, respectively. To accoplish the purpose, the following were the particular subjects.
1.The enhancement of oligosaccharide formation ability of -gal 1 by chemical modification.
2.Immobilization of -Gal 1 and 2 and elucidation of their properties.
3.The stability of immobilyzed enzyme during continuous reaction.
4.Long term continuous oligosuccharide production using either prug flow reactor or membrane reactor.
5.Protection against con … More tamination and cleaning of immobilized enzyme column reactor.
By treating the -Gal 1 with 0.01-3% glutaraldehyde, the amino group on the enzyme was modified from 0 to 90%. With increase in modification, increased the ability to form galacto-oligosaccharides of degree of polymerization two to five containing a glucose residue and yield of oligosaccharide from lactose reached to 40% with amino group modification 90%. Either -GAl 2 or -Gal 1 was adosorbed on to various suports and immobilized by glutaraldehyde crosslinking. Among the supports tested, Merckogel was most suitable with respect to activity and stability. however higher the specific activity, easer the immobilized enzyme deactivated reversibly. The reason for this phenomena was ascribed to the entrapment of oligosaccharides produced in the three dimensional network of crosslinked enzymes. Continuous oligosaccharide production was performed in PFR with immobilized enzyme on to merckogel SI-500(15U/g) and in membrane reactor(Diaflo cell, UF-X50) with free enzyme for 8 days without enzyme inactivation and the oligosaccharide yield from 20% lactose was maintained at 47.5%. From the adsorption-desorption experiments of milk protein, the support suitable with respect to the protection of contamination and cleaning was searched. Ion exchanger with the charge of same sign as contaminant was effective. The suggestion was obtained that the growth of micro-organism was reduced by usinglarge support with high flow rate. Less

Report

(3 results)
  • 1988 Annual Research Report   Final Research Report Summary
  • 1987 Annual Research Report
  • Research Products

    (12 results)

All Other

All Publications (12 results)

  • [Publications] Z.Mozaffar.: Appl.Microbiol Biotechnol.25. 426-429 (1987)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1988 Final Research Report Summary
  • [Publications] Z.Mozaffar.: Biotechnology Letters. 10. 805-808 (1988)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1988 Final Research Report Summary
  • [Publications] Z.Mozaffar.: Appl.Microbiol.Biotechnol.(1989)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1988 Final Research Report Summary
  • [Publications] 中西一弘: "バイオリアクター(バイオリアクター研究会編)6章2節 ラクターゼによるガラクトオリゴ糖の生産" 株式会社アイピーシー, 12 (1988)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1988 Final Research Report Summary
  • [Publications] Z. Mozaffar: "Effect of glutaraldehyde on oligosaccharide production by -galactosidase from Bacillus circulans" Appl. Microbiol. Biotechnol.25. 426-429 (1987)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1988 Final Research Report Summary
  • [Publications] Z. Mozaffar: "Production of oligosaccharides by glutaraldehyde treated and immobilized beta-galactosidases from Bacillus cirulans" Biotechnology Letters. 10. 805-808 (1988)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1988 Final Research Report Summary
  • [Publications] Z. Mozaffar: "Production of trisaccharides from lactose using beta-galactosidase from Bacillus circulans modified by glutaraldhyde" Appl. Microbiol. Biotechnol.(1989)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1988 Final Research Report Summary
  • [Publications] K. Nakanishi: Bioreator(ed. by research association of bioreactor, Societyof Chemcal Eng. Japan) Chap. 6 sec. 2 Galacto-oligosaccharides production by lactase. Industrial Publishing & Consulting, Inc., 12 (1988)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1988 Final Research Report Summary
  • [Publications] Z.Mozaffar: Biotechnology Letters. 10. 805-808 (1988)

    • Related Report
      1988 Annual Research Report
  • [Publications] Z.Mozaffar: Appl.Microbiol.Biotechnol.(1989)

    • Related Report
      1988 Annual Research Report
  • [Publications] Z. Mozaffar: Appl. Microbiol. Biotechnol. 25. 426-429 (1987)

    • Related Report
      1987 Annual Research Report
  • [Publications] 中西一弘: "バイオリアクター(バイオリアクター研究会編)6章2節ラクターゼによるガラクトオリゴ糖の生産" 株式会社アイビーシー, 12 (1988)

    • Related Report
      1987 Annual Research Report

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Published: 1987-04-01   Modified: 2016-04-21  

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